[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 96604 / S288c / FY1679; DOI=10.1038/369371a0; PubMed=8196765 [NCBI, ExPASy, EBI, Israel, Japan] Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.; "Complete DNA sequence of yeast chromosome XI."; Nature 369:371-378(1994).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 204508 / S288c; DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan] Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.; "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."; Genome Res. 17:536-543(2007).
[3]	SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan] Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.; "Global analysis of protein localization in budding yeast."; Nature 425:686-691(2003).
[4]	LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan] Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.; "Global analysis of protein expression in yeast."; Nature 425:737-741(2003).
[5]	FUNCTION, INDUCTION, DISULFIDE BOND WITH TSA1, AND MUTAGENESIS OF CYS-48; CYS-84 AND CYS-106. DOI=10.1038/nature02075; PubMed=14586471 [NCBI, ExPASy, EBI, Israel, Japan] Biteau B., Labarre J., Toledano M.B.; "ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin."; Nature 425:980-984(2003).

Comments

FUNCTION: Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxin TSA1. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and as thioltransferase.
CATALYTIC ACTIVITY: Peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH = peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R.
COFACTOR: Magnesium.
INTERACTION:
P40073:SSU81; NbExp=1; IntAct=EBI-26774, EBI-18140;
SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
INDUCTION: By hydrogen peroxide.
PTM: Forms a transient disulfide bond with TSA1 during the reduction of cysteine sulfinic acid (-SO2H).
MISCELLANEOUS: Present with 538 molecules/cell in log phase SD medium.
SIMILARITY: Belongs to the sulfiredoxin family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z28086; CAA81924.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY558350; AAS56676.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S37911; S37911.

RefSeq

NP_012837.1; -.

3D structure databases

ModBase

P36077.

Protein-protein interaction databases

DIP

DIP:4344N; -.

IntAct

P36077; -.

Organism-specific databases

YKL086w; -.

S000001569; SRX1.

Gene expression databases

GermOnline

YKL086W; Saccharomyces cerevisiae.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0016209;	Molecular function: antioxidant activity (inferred from electronic annotation from UniProtKB-KW).
GO:0003677;	Molecular function: DNA binding (inferred from electronic annotation from InterPro).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0032542;	Molecular function: sulfiredoxin activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006979;	Biological process: response to oxidative stress (inferred from mutant phenotype from SGD).
QuickGo view.

Family and domain databases

InterPro

IPR003115; ParBc.
IPR016692; Sulfiredoxin.
Graphical view of domain structure.

Pfam

PF02195; ParBc; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF017267; Sulfiredoxin; 1.

SMART

SM00470; ParB; 1.
SMART graphical view of domain structure.

ProtoNet

P36077.

Genome annotation databases

Ensembl

YKL086W; Saccharomyces cerevisiae. [Contig view]

853776; -.

Y13137_GR; YKL086W.

sce:YKL086W; -.

fig|4932.3.peg.3821; -.

Phylogenomic databases

HOGENOM

P36077; -.

Other

LinkHub

P36077; -.

NextBio

974885; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Antioxidant; Complete proteome; Cytoplasm; Magnesium; Nucleus; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 127`	`127`	`Sulfiredoxin.`	`PRO_0000211435`
`DISULFID`	`84 84`		`Interchain (with C-48 in TSA1); transient.`
`MUTAGEN`	`48 48`		`C->S: Minor effect on formation of disulfide bond with TSA1 and reduction of cysteine-sulfinic acid.`
`MUTAGEN`	`84 84`		`C->S: Abolishes formation of disulfide bond with TSA1 and reduction of cysteine-sulfinic acid.`
`MUTAGEN`	`106 106`		`C->S: No effect on formation of disulfide bond with TSA1 and reduction of cysteine-sulfinic acid.`

Sequence information

Length: 127 AA [This is the length of the unprocessed precursor]

Molecular weight: 13854 Da [This is the MW of the unprocessed precursor]

CRC64: AC15AFD2F6CBC9A0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSLQSNSVKP TEIPLSEIRR PLAPVLDPQK IDAMVATMKG IPTASKTCSL EQAEAAASAG 

        70         80         90        100        110        120 
ELPPVDVLGV RVKGQTLYYA FGGCHRLQAY DRRARETQNA AFPVRCRVLP ATPRQIRMYL 


GSSLDIE

P36077 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools